A novel Ser O-glucuronidation in acidic proline-rich proteins identified by tandem mass spectrometry. | |
MedLine Citation:
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PMID: 10858503 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Human acidic proline-rich salivary protein PRP-1 and its C-terminally truncated form PRP-3 were analyzed by electrospray tandem mass spectrometry. Post-translational modifications were detected and characterized. A pyroglutamic acid residue was demonstrated at the N-terminus, Ser-8 and Ser-22 were shown to be phosphorylated and an O-linked glucuronic acid conjugation was identified. The latter modification was located to Ser-17 and found to be present in approximately 40% of the polypeptides. |
Authors:
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A P Jonsson; W J Griffiths; P Bratt; I Johansson; N Strömberg; H Jörnvall; T Bergman |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: FEBS letters Volume: 475 ISSN: 0014-5793 ISO Abbreviation: FEBS Lett. Publication Date: 2000 Jun |
Date Detail:
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Created Date: 2000-07-24 Completed Date: 2000-07-24 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 131-4 Citation Subset: IM |
Affiliation:
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Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden. |
Export Citation:
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MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Chromatography, High Pressure Liquid Glucuronic Acid / metabolism* Humans Mass Spectrometry / methods* Molecular Sequence Data Peptides / chemistry*, isolation & purification, metabolism Proline / chemistry Proline-Rich Protein Domains Protein Processing, Post-Translational Serine / metabolism* Time Factors Trypsin / metabolism |
Chemical | |
Reg. No./Substance:
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0/Peptides; 147-85-3/Proline; 56-45-1/Serine; 576-37-4/Glucuronic Acid; EC 3.4.21.4/Trypsin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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